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Volumn 22, Issue 5, 2011, Pages 923-930

Fluorescence-quenching screening of protein kinase C ligands with an environmentally sensitive fluorophore

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ENZYMES; FLUORESCENCE QUENCHING; FLUOROPHORES; LEAD COMPOUNDS;

EID: 80053008558     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc100567k     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 74049147038 scopus 로고    scopus 로고
    • Monitoring protein interactions and dynamics with solvatochromic fluorophores
    • Loving, G. S., Sainlos, M., and Imperiali, B. (2010) Monitoring protein interactions and dynamics with solvatochromic fluorophores. Trends Biotechnol. 28, 73-83.
    • (2010) Trends Biotechnol , vol.28 , pp. 73-83
    • Loving, G.S.1    Sainlos, M.2    Imperiali, B.3
  • 2
    • 24344456096 scopus 로고    scopus 로고
    • Chemical approaches for investigating phosphorylation in signal transduction networks
    • DOI 10.1016/j.tcb.2005.07.003, PII S0962892405001819
    • Rothman, D. M., Shults, M. D., and Imperiali, B. (2005) Chemical approaches for investigating phosphorylation in signal transduction networks. Trends Cell Biol. 15, 502-510. (Pubitemid 41253470)
    • (2005) Trends in Cell Biology , vol.15 , Issue.9 , pp. 502-510
    • Rothman, D.M.1    Shults, M.D.2    Imperiali, B.3
  • 3
    • 53849087812 scopus 로고    scopus 로고
    • Fluorescent probes for bioimaging applications
    • Terai, T., and Nagano, T. (2008) Fluorescent probes for bioimaging applications. Curr. Opin. Chem. Biol. 12, 515-521.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 515-521
    • Terai, T.1    Nagano, T.2
  • 4
    • 47249098333 scopus 로고    scopus 로고
    • Substrate arrays for fluorescence-based enzyme fingerprinting and high-throughput screening
    • DOI 10.1196/annals.1430.000, Fluorescence Methods and Applications: Spectroscopy, Imaging, and Probes
    • Reymond, J. -L. (2008) Substrate arrays for fluorescence-based enzyme fingerprinting and high-throughput screening. Ann. N.Y. Acad. Sci. 1130, 12-20. (Pubitemid 351990230)
    • (2008) Annals of the New York Academy of Sciences , vol.1130 , pp. 12-20
    • Reymond, J.-L.1
  • 5
    • 52249114490 scopus 로고    scopus 로고
    • Fluorophore labeling enables imaging and evaluation of specific CXCR4-ligand interaction at the cell membrane for fluorescence-based screening
    • Nomura, W., Tanabe, Y., Tsutsumi, H., Tanaka, T., Ohba, K., Yamamoto, N., and Tamamura, H. (2008) Fluorophore labeling enables imaging and evaluation of specific CXCR4-ligand interaction at the cell membrane for fluorescence-based screening. Bioconjugate Chem. 19, 1917-1920.
    • (2008) Bioconjugate Chem , vol.19 , pp. 1917-1920
    • Nomura, W.1    Tanabe, Y.2    Tsutsumi, H.3    Tanaka, T.4    Ohba, K.5    Yamamoto, N.6    Tamamura, H.7
  • 6
    • 35948989378 scopus 로고    scopus 로고
    • Surface recognition and fluorescence sensing of histone by dansyl-appended cyclophane-based resorcinarene trimer
    • DOI 10.1021/ja074906h
    • Hayashida, O., Ogawa, N., and Uchiyama, M. (2007) Surface recognition and fluorescence sensing of histone by dansyl-appended cyclophane-based resorcinarene trimer. J. Am. Chem. Soc. 129, 13698-13705. (Pubitemid 350071799)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.44 , pp. 13698-13705
    • Hayashida, O.1    Ogawa, N.2    Uchiyama, M.3
  • 8
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. (1992) Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Sceince 258, 607-614.
    • (1992) Sceince , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 9
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A. C. (1995) Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270, 28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 11
    • 0027292678 scopus 로고
    • Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-α and -δ and not by protein kinase C-βII, -ε, -ζ, and -η
    • Mischak, H., Pierce, J. H., Goodnight, J., Kazanietz, M. G., Blumberg, P. M., and Mushinski, J. F. (1993) Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-alpha and -delta and not by protein kinase C-beta II, -epsilon, -zeta, and -eta. J. Biol. Chem. 268, 20110-20115. (Pubitemid 23278909)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.27 , pp. 20110-20115
    • Mischak, H.1    Pierce, J.H.2    Goodnight, J.3    Kazanietz, M.G.4    Blumberg, P.M.5    Mushinski, J.F.6
  • 12
    • 0642303674 scopus 로고    scopus 로고
    • Mechanical stress-activated PKCdelta regulates smooth muscle cell migration
    • Li, C., Wernig, F., Leitges, M., Hu, Y., and Xu, Q. (2003) Mechanical stress-activated PKCdelta regulates smooth muscle cell migration. FASEB J. 17, 2106-2108.
    • (2003) FASEB J. , vol.17 , pp. 2106-2108
    • Li, C.1    Wernig, F.2    Leitges, M.3    Hu, Y.4    Xu, Q.5
  • 14
    • 33846528583 scopus 로고    scopus 로고
    • PKC signaling deficits: A mechanistic hypothesis for the origins of Alzheimer's disease
    • DOI 10.1016/j.tips.2006.12.002, PII S0165614706002859
    • Alkon, D. L., Sun, M.-K., and Nelson, T. J. (2007) PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease. Trends Pharmacol. Sci. 28, 51-60. (Pubitemid 46161834)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.2 , pp. 51-60
    • Alkon, D.L.1    Sun, M.-K.2    Nelson, T.J.3
  • 15
    • 33744926666 scopus 로고    scopus 로고
    • PKD at the crossroads of DAG and PKC signaling
    • DOI 10.1016/j.tips.2006.04.003, PII S0165614706001040
    • Wang, Q. J. (2006) PKD at the crossroads of DAG and PKC signaling. Trends Pharmacol. Sci. 27, 317-323. (Pubitemid 43850003)
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.6 , pp. 317-323
    • Wang, Q.J.1
  • 16
    • 0038679456 scopus 로고    scopus 로고
    • Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C)
    • Marquez, V. E., and Blumberg, P. M. (2003) Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C). Acc. Chem. Res. 36, 434-443.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 434-443
    • Marquez, V.E.1    Blumberg, P.M.2
  • 17
    • 0034624775 scopus 로고    scopus 로고
    • Conformationally constrained analogues of diacylglycerol (DAG). 16. How much structural complexity is necessary for recognition and high binding affinity to protein kinase C?
    • DOI 10.1021/jm9904607
    • Nacro, K., Bienfait, B., Lee, J., Han, K.-C., Kang, J.-H., Benzaria, S., Lewin, N. E., Bhattacharyya, D. K., Blumberg, P. M., and Marquez, V. E. (2000) Conformationally constrained analogues of diacylglycerol (DAG). 16. How much structural complexity is necessary for recognition and high binding affinity to protein kinase C?. J. Med. Chem. 43, 921-944. (Pubitemid 30152299)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.5 , pp. 921-944
    • Nacro, K.1    Bienfait, B.2    Lee, J.3    Han, K.-C.4    Kang, J.-H.5    Benzaria, S.6    Lewin, N.E.7    Bhattacharyya, D.K.8    Blumberg, P.M.9    Marquez, V.E.10
  • 18
    • 0034710703 scopus 로고    scopus 로고
    • Conformationally constrained analogues of diacylglycerol (DAG). 17. Contrast between sn-1 and sn-2 DAG lactones in binding to protein kinase C
    • Tamamura, H., Bienfait, B., Nacro, K., Lewin, N. E., Blumberg, P. M., and Marquez, V. E. (2000) Conformationally constrained analogues of diacylglycerol (DAG). 17. Contrast between sn-1 and sn-2 DAG lactones in binding to protein kinase C. J. Med. Chem. 43, 3209-3217.
    • (2000) J. Med. Chem. , vol.43 , pp. 3209-3217
    • Tamamura, H.1    Bienfait, B.2    Nacro, K.3    Lewin, N.E.4    Blumberg, P.M.5    Marquez, V.E.6
  • 19
    • 1642458686 scopus 로고    scopus 로고
    • Conformationally Constrained Analogues of Diacylglycerol. 20. The Search for an Elusive Binding Site on Protein Kinase C through Relocation of the Carbonyl Pharmacophore Along the sn-1 Side Chain of 1,2-Diacylglycerol Lactones
    • DOI 10.1021/jm030454h
    • Tamamura, H., Sigano, D. M., Lewin, N. E., Blumberg, P. M., and Marquez, V. E. (2004) Conformationally constrained analogues of diacylglycerol. 20. The search for an elusive binding site on protein kinase C through relocation of the carbonyl pharmacophore along the sn-1 side chain of 1,2-diacylglycerol lactones. J. Med. Chem. 47, 644-655. (Pubitemid 38129721)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.3 , pp. 644-655
    • Tamamura, H.1    Sigano, D.M.2    Lewin, N.E.3    Blumberg, P.M.4    Marquez, V.E.5
  • 21
    • 2342643572 scopus 로고    scopus 로고
    • Evaluation of series of isobenzofuranone dimers as PKCα ligands: Implication for the distance between the two ligand binding sites
    • DOI 10.1016/j.bmcl.2004.02.098, PII S0960894X04003385
    • Baba, Y., Mayumi, S., Hirai, G., Kawasaki, H., Ogoshi, Y., Yanagisawa, T., Hashimoto, Y., and Sodeoka, M. (2004) Evaluation of series of isobenzofuranone dimers as PKCalpha ligands: implication for the distance between the two ligand binding sites. Bioorg. Med. Chem. Lett. 14, 2969-2972. (Pubitemid 38569774)
    • (2004) Bioorganic and Medicinal Chemistry Letters , vol.14 , Issue.11 , pp. 2969-2972
    • Baba, Y.1    Mayumi, S.2    Hirai, G.3    Kawasaki, H.4    Ogoshi, Y.5    Yanagisawa, T.6    Hashimoto, Y.7    Sodeoka, M.8
  • 22
    • 37849047968 scopus 로고    scopus 로고
    • Synthesis, conformational analysis, and biological evaluation of 1-hexylindolactam-V10 as a selective activator for novel protein kinase C isozymes
    • Yanagita, R. C., Nakagawa, Y., Yamanaka, N., Kashiwagi, K., Saito, N., and Irie, K. (2008) Synthesis, conformational analysis, and biological evaluation of 1-hexylindolactam-V10 as a selective activator for novel protein kinase C isozymes. J. Med. Chem. 51, 46-56.
    • (2008) J. Med. Chem. , vol.51 , pp. 46-56
    • Yanagita, R.C.1    Nakagawa, Y.2    Yamanaka, N.3    Kashiwagi, K.4    Saito, N.5    Irie, K.6
  • 23
    • 67650558672 scopus 로고    scopus 로고
    • A simple analogue of tumor-promoting aplysiatoxin is an antineoplastic agent rather than a tumor promoter: Development of a synthetically accessible protein kinase C activator with bryostatin-like activity
    • Nakagawa, Y., Yanagita, R. C., Hamada, N., Murakami, A., Takahashi, H., Saito, N., Nagai, H., and Irie, K. (2009) A simple analogue of tumor-promoting aplysiatoxin is an antineoplastic agent rather than a tumor promoter: development of a synthetically accessible protein kinase C activator with bryostatin-like activity. J. Am. Chem. Soc. 131, 7573-7579.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7573-7579
    • Nakagawa, Y.1    Yanagita, R.C.2    Hamada, N.3    Murakami, A.4    Takahashi, H.5    Saito, N.6    Nagai, H.7    Irie, K.8
  • 24
    • 0027989427 scopus 로고
    • General method for the synthesis of phospholipid derivatives of 1,2-O-diacyl-sn-glycerols
    • Martin, S. F., Josey, J. A., Wong, Y.-L., and Dean, D. W. (1994) General method for the synthesis of phospholipid derivatives of 1,2-Odiacyl-sn- glycerols. J. Org. Chem. 59, 4805-4820. (Pubitemid 24291838)
    • (1994) Journal of Organic Chemistry , vol.59 , Issue.17 , pp. 4805-4820
    • Martin, S.F.1    Josey, J.A.2    Wong, Y.-L.3    Dean, D.W.4
  • 25
    • 33847771003 scopus 로고    scopus 로고
    • Conformationally constrained analogues of diacylglycerol (DAG). 27. Modulation of membrane translocation of protein kinase C (PKC) isozymes α and δ by diacylglycerol lactones (DAG-lactones) containing rigid-rod acyl groups
    • DOI 10.1021/jm061289j
    • Malolanarasimhan, K., Kedei, N., Sigano, D. M., Kelley, J. A., Lai, C. C., Lewin, N. E., Surawski, R. J., Pavlyukovets, V. A., Garfield, S. H., Wincovitch, S., Blumberg, P. M., and Marquez, V. E. (2007) Conformationally constrained analogues of diacylglycerol (DAG). 27. Modulation of membrane translocation of protein kinase C (PKC) isozymes alpha and delta by diacylglycerol lactones (DAG-lactones) containing rigid-rod acyl groups. J. Med. Chem. 50, 962-978. (Pubitemid 46393999)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.5 , pp. 962-978
    • Malolanarasimhan, K.1    Kedei, N.2    Sigano, D.M.3    Kelley, J.A.4    Lai, C.C.5    Lewin, N.E.6    Surawski, R.J.7    Pavlyukovets, V.A.8    Garfield, S.H.9    Wincovitch, S.10    Blumberg, P.M.11    Marquez, V.E.12
  • 27
    • 0025781579 scopus 로고
    • Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: Sequence of the cDNA, expression patterns, and characterization of the protein
    • Mischak, H., Bodenteich, A., Kolch, W., Goodnight, J., Hofer, F., and Mushinski, J. F. (1991) Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns, and characterization of the protein. Biochemistry 30, 7925-7931.
    • (1991) Biochemistry , vol.30 , pp. 7925-7931
    • Mischak, H.1    Bodenteich, A.2    Kolch, W.3    Goodnight, J.4    Hofer, F.5    Mushinski, J.F.6
  • 28
    • 0026779291 scopus 로고
    • Differential irreversible insertion of protein kinase C into phospholipid vesicles by phorbol esters and related activators
    • Kazanietz, M. G., Krausz, K. W., and Blumberg, P. M. (1992) Differential irreversible insertion of protein kinase C into phospholipid vesicles by phorbol esters and related activators. J. Biol. Chem. 267, 20878-20886.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20878-20886
    • Kazanietz, M.G.1    Krausz, K.W.2    Blumberg, P.M.3
  • 30
    • 0000142013 scopus 로고
    • Dansylglycine as a fluorescent probe for aqueous solutions of cationic detergents
    • Davis, G. A. (1972) Dansylglycine as a fluorescent probe for aqueous solutions of cationic detergents. J. Am. Chem. Soc. 94, 5089-5090.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 5089-5090
    • Davis, G.A.1
  • 32
    • 0033562361 scopus 로고    scopus 로고
    • A real-time fluorescence method to monitor the melting of duplex DNA during transcription initiation by RNA polymerase
    • DOI 10.1006/abio.1999.4078
    • Matlock, D. L., and Heyduk, T. (1999) A real-time fluorescence method to monitor the melting of duplex DNA during transcription initiation by RNA polymerase. Anal. Biochem. 270, 140-147. (Pubitemid 29230730)
    • (1999) Analytical Biochemistry , vol.270 , Issue.1 , pp. 140-147
    • Matlock, D.L.1    Heyduk, T.2
  • 33
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid
    • Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., and Matsuzaki, K. (2001) Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276, 24985-24990.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 34
    • 0037199492 scopus 로고    scopus 로고
    • Isoform-selective interaction of cyclooxygenase-2 with indomethacin amides studied by real-time fluorescence, inhibition kinetics, and site-directed mutagenesis
    • DOI 10.1021/bi0203637
    • Timofeevski, S. L., Prusakiewicz, J. J., Rouzer, C. A., and Marnett, L. J. (2002) Isoform-selective interaction of cyclooxygenase-2 with indomethacin amides studied by real-time fluorescence, inhibition kinetics, and site-directed mutagenesis. Biochemistry 41, 9654-9662. (Pubitemid 34810040)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9654-9662
    • Timofeevski, S.L.1    Prusakiewicz, J.J.2    Rouzer, C.A.3    Marnett, L.J.4
  • 35
    • 47749106134 scopus 로고    scopus 로고
    • Supramolecular control of split-GFP reassembly by conjugation of β-cyclodextrin and coumarin units
    • DOI 10.1021/ja802313a
    • Sakamoto, S., and Kudo, K. (2008) Supramolecular control of split-GFP reassembly by conjugation of beta-cyclodextrin and coumarin units. J. Am. Chem. Soc. 130, 9574-9582. (Pubitemid 352031170)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.29 , pp. 9574-9582
    • Sakamoto, S.1    Kudo, K.2
  • 36
    • 0021967116 scopus 로고
    • 3H]phorbol 12,13-dibutyrate binding
    • Sharkey, N. A., and Blumberg, P. M. (1985) Highly lipophilic phorbol esters as inhibitors of specific [3H]phorbol 12,13-dibutyrate binding. Cancer Res. 45, 19-24. (Pubitemid 15196924)
    • (1985) Cancer Research , vol.45 , Issue.1 , pp. 19-24
    • Sharkey, N.A.1    Blumberg, P.M.2
  • 37
    • 70449641245 scopus 로고    scopus 로고
    • Synthesis of protein kinase Cdelta C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding
    • Ohashi, N., Nomura, W., Kato, M., Narumi, T., Lewin, N. E., Blumberg, P. M., and Tamamura, H. (2009) Synthesis of protein kinase Cdelta C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding. J. Pept. Sci. 15, 642-646.
    • (2009) J. Pept. Sci. , vol.15 , pp. 642-646
    • Ohashi, N.1    Nomura, W.2    Kato, M.3    Narumi, T.4    Lewin, N.E.5    Blumberg, P.M.6    Tamamura, H.7


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